AREG Human

Amphiregulin Human Recombinant
Cat. No.
BT8947
Source
Escherichia Coli.
Synonyms
Schwannoma-derived growth factor, Colorectum cell-derived growth factor, AR, CRDGF, SDGF, AREGB, MGC13647.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 95.0% as determined by:
(a) Analysis by HPLC.
(b) Analysis by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

Amphiregulin (AREG) Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 98 amino acids and having a molecular mass of 11.3 KDa.
The AREG is purified by proprietary chromatographic techniques.

Product Specs

Description
Recombinant Human Amphiregulin (AREG) is a single, non-glycosylated polypeptide chain produced in E. coli. It contains 98 amino acids and has a molecular mass of 11.3 kDa. AREG is purified using proprietary chromatographic techniques.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation
Lyophilized from a 0.2 µm filtered concentrated solution in phosphate-buffered saline (PBS) at pH 7.4.
Solubility
To reconstitute the lyophilized AREG, it is recommended to dissolve it in sterile 18 MΩ-cm H₂O at a concentration of at least 100 µg/ml. Further dilutions can be made in other aqueous solutions.
Stability
Lyophilized AREG is stable at room temperature for 3 weeks. However, for long-term storage, it is recommended to store it desiccated below -18°C. Once reconstituted, AREG should be stored at 4°C for 2-7 days. For future use, it should be stored below -18°C. The addition of a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
The purity is greater than 95.0% as determined by: (a) High-performance liquid chromatography (HPLC) analysis and (b) Sodium dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis.
Biological Activity
The biological activity of AREG is determined by its ability to stimulate the proliferation of mouse Balb/c 3T3 cells. The expected half-maximal effective concentration (ED₅₀) for this effect is 5-10 ng/ml, corresponding to a specific activity of 100,000-200,000 units/mg.
Synonyms
Schwannoma-derived growth factor, Colorectum cell-derived growth factor, AR, CRDGF, SDGF, AREGB, MGC13647.
Source
Escherichia Coli.
Amino Acid Sequence
SVRVEQVVKP PQNKTESENT SDKPKRKKKG GKNGKNRRNR KKKNPCNAEF QNFCIHGECK YIEHLEAVTC KCQQEYFGER CGEKSMKTHS MIDSSLSK.

Product Science Overview

Structure and Expression

The AR cDNA encodes a 252 amino acid (aa) residue transmembrane precursor . Multiple forms of native AR containing either 78 or 84 aa residues and both N- and O-linked oligosaccharides have been identified . Amphiregulin is expressed in various parts of the body, including the ovary, placenta, pancreas, breast, lung, and spleen .

Biological Functions

Amphiregulin interacts with the epidermal growth factor receptor (EGFR) to promote the growth of normal epithelial cells . It plays a crucial role in mammary ductal development and has been implicated in driving human breast cancer progression . Additionally, it drives the proliferation of fibroblasts and the production of cytokines such as interleukin 8 (IL-8) and vascular endothelial growth factor (VEGF), suggesting a proinflammatory role observed in conditions like rheumatoid arthritis .

Recombinant Human Amphiregulin

Recombinant human Amphiregulin is typically produced in E. coli and is supplied in a lyophilized form . It is used in various research applications, including cell proliferation assays. The bioactivity of recombinant human Amphiregulin is determined in a 3T3 cell proliferation assay, with an effective dose (ED50) of less than or equal to 20 ng/mL .

Applications and Storage

Recombinant human Amphiregulin is used in cell or tissue culture and as an ELISA standard . It is recommended to reconstitute the lyophilized protein in sterile water or PBS, with the addition of a carrier protein like BSA for long-term storage . The stability and storage conditions vary, but it is generally stable for 12 months at -20 to -70°C as supplied, and for 1 to 3 months after reconstitution under sterile conditions .

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